SitesBLAST
Comparing Ga0059261_4052 FitnessBrowser__Korea:Ga0059261_4052 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
68% identity, 98% coverage: 6:382/385 of query aligns to 6:375/377 of 4ktoA
- active site: M130 (= M131), S131 (= S132), E239 (= E246), A360 (= A367), R372 (= R379)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), M155 (≠ F161), W156 (= W162), T158 (= T164), R265 (= R272), F268 (= F275), I272 (= I279), F275 (= F282), M278 (= M285), Q333 (= Q340), A334 (= A341), G337 (= G344), L355 (= L362), G359 (= G366), T362 (= T369), E364 (= E371)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
58% identity, 96% coverage: 10:379/385 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S132), G140 (= G137), S141 (= S138), W165 (= W162), T167 (= T164), R279 (= R272), F282 (= F275), I286 (= I279), F289 (= F282), Q347 (= Q340), C348 (≠ A341), G351 (= G344), L369 (= L362), G375 (= G368), T376 (= T369), L382 (≠ M375)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
58% identity, 96% coverage: 10:379/385 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M131), S131 (= S132), E249 (= E246), A370 (= A367), R382 (= R379)
- binding coenzyme a persulfide: S137 (= S138), S185 (= S182), R186 (= R183), V239 (= V236), Y240 (≠ G237), M243 (= M240), E249 (= E246), R250 (= R247), G369 (= G366), A370 (= A367), G371 (= G368), V375 (≠ I372)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), R275 (= R272), F278 (= F275), F285 (= F282), M288 (= M285), Q343 (= Q340), C344 (≠ A341), G347 (= G344), T372 (= T369), E374 (= E371)
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
58% identity, 96% coverage: 10:379/385 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 129:138, 80% identical) binding
- S174 (= S138) binding
- WIT 198:200 (= WIT 162:164) binding
- SR 222:223 (= SR 182:183) binding
- G250 (= G210) to A: in IVA; uncertain significance
- Y277 (≠ G237) binding
- DLER 284:287 (≠ DYER 244:247) binding
- E286 (= E246) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (= A251) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R272) binding
- Q323 (= Q283) binding
- I379 (≠ V339) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QALGG 340:344) binding
- R398 (= R358) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ L363) to N: in IVA; uncertain significance
- A407 (= A367) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 367:368) binding
- TSE 409:411 (≠ TNE 369:371) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
41% identity, 98% coverage: 6:382/385 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ M131), T126 (≠ S132), G242 (≠ E246), E363 (≠ A367), R375 (= R379)
- binding coenzyme a persulfide: T132 (≠ S138), H179 (≠ R183), F232 (≠ V236), M236 (= M240), E237 (≠ S241), L239 (= L243), D240 (= D244), R243 (= R247), Y362 (≠ G366), E363 (≠ A367), G364 (= G368), R375 (= R379)
- binding flavin-adenine dinucleotide: F123 (≠ L129), L125 (≠ M131), T126 (≠ S132), G131 (= G137), T132 (≠ S138), F156 (≠ W162), I157 (= I163), T158 (= T164), R268 (= R272), Q270 (= Q274), F271 (= F275), I275 (= I279), F278 (= F282), L281 (≠ M285), Q336 (= Q340), I337 (≠ A341), G340 (= G344), I358 (≠ L362), Y362 (≠ G366), T365 (= T369), Q367 (≠ E371)
- binding 1,3-propandiol: L5 (= L10), Q10 (≠ E15)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
41% identity, 97% coverage: 11:382/385 of query aligns to 5:377/378 of 5ol2F
- active site: L124 (≠ M131), T125 (≠ S132), G241 (≠ E246), G374 (≠ R379)
- binding calcium ion: E29 (≠ K35), E33 (= E39), R35 (≠ W41)
- binding coenzyme a persulfide: L238 (= L243), R242 (= R247), E362 (≠ A367), G363 (= G368)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), T125 (≠ S132), P127 (≠ A134), T131 (≠ S138), F155 (≠ W162), I156 (= I163), T157 (= T164), E198 (≠ I203), R267 (= R272), F270 (= F275), L274 (≠ I279), F277 (= F282), Q335 (= Q340), L336 (≠ A341), G338 (= G343), G339 (= G344), Y361 (≠ G366), T364 (= T369), E366 (= E371)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 97% coverage: 10:382/385 of query aligns to 34:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
41% identity, 97% coverage: 10:382/385 of query aligns to 7:380/384 of 1jqiA
- active site: G377 (≠ R379)
- binding acetoacetyl-coenzyme a: L95 (= L99), F125 (≠ L129), S134 (= S138), F234 (≠ V236), M238 (= M240), Q239 (≠ S241), L241 (= L243), D242 (= D244), R245 (= R247), Y364 (≠ G366), E365 (≠ A367), G366 (= G368)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R272), F273 (= F275), L280 (≠ F282), Q338 (= Q340), I339 (≠ A341), G342 (= G344), I360 (≠ L362), T367 (= T369), E369 (= E371), I370 (= I372)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
41% identity, 97% coverage: 10:382/385 of query aligns to 34:407/412 of P16219
- G90 (= G67) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E81) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 129:138, 60% identical) binding in other chain
- R171 (≠ E148) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 162:164) binding in other chain
- A192 (= A169) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G184) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R272) binding
- Q308 (= Q283) binding in other chain
- R325 (= R300) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S328) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QALGG 340:344) binding
- R380 (= R355) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 369:371) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 97% coverage: 10:382/385 of query aligns to 7:380/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ A345), T347 (≠ K349), E348 (≠ D350)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R272), F273 (= F275), L280 (≠ F282), V282 (≠ L284), Q338 (= Q340), I339 (≠ A341), G342 (= G344), I360 (≠ L362), Y364 (≠ G366), T367 (= T369), E369 (= E371), I370 (= I372), L373 (≠ M375)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 97% coverage: 10:382/385 of query aligns to 10:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L129), L130 (≠ M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), T214 (= T213), R273 (= R272), F276 (= F275), L280 (≠ I279), L283 (≠ F282), V285 (≠ L284), Q341 (= Q340), I342 (≠ A341), G345 (= G344), I363 (≠ L362), Y367 (≠ G366), T370 (= T369), E372 (= E371), L376 (≠ M375)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
41% identity, 97% coverage: 10:382/385 of query aligns to 4:377/381 of 8sgsA
- binding coenzyme a: S131 (= S138), A133 (≠ V140), N177 (≠ S182), F231 (≠ V236), M235 (= M240), L238 (= L243), I312 (≠ R317), E362 (≠ A367), G363 (= G368)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), T157 (= T164), R267 (= R272), F270 (= F275), L274 (≠ I279), L277 (≠ F282), Q335 (= Q340), I336 (≠ A341), G338 (= G343), G339 (= G344), I357 (≠ L362), I360 (= I365), Y361 (≠ G366), T364 (= T369), E366 (= E371)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
40% identity, 96% coverage: 16:383/385 of query aligns to 8:374/374 of 5lnxD
- active site: L122 (≠ M131), T123 (≠ S132), G239 (≠ E246), E358 (≠ A367), K370 (≠ R379)
- binding flavin-adenine dinucleotide: L122 (≠ M131), T123 (≠ S132), G128 (= G137), S129 (= S138), F153 (≠ W162), T155 (= T164), R265 (= R272), Q267 (= Q274), F268 (= F275), I272 (= I279), N275 (≠ F282), I278 (≠ M285), Q331 (= Q340), I332 (≠ A341), G335 (= G344), Y357 (≠ G366), T360 (= T369), E362 (= E371)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
40% identity, 97% coverage: 10:382/385 of query aligns to 1:367/371 of 2vigB
- active site: L121 (≠ M131), S122 (= S132), G231 (≠ E246), E352 (≠ A367), G364 (≠ R379)
- binding coenzyme a persulfide: S128 (= S138), F221 (≠ V236), M225 (= M240), Q226 (≠ S241), L228 (= L243), D229 (= D244), R232 (= R247), E352 (≠ A367), G353 (= G368), I357 (= I372)
- binding flavin-adenine dinucleotide: L121 (≠ M131), S122 (= S132), G127 (= G137), S128 (= S138), W152 (= W162), T154 (= T164), R257 (= R272), F260 (= F275), L264 (≠ I279), L267 (≠ F282), Q325 (= Q340), I326 (≠ A341), G329 (= G344), I347 (≠ L362), Y351 (≠ G366), T354 (= T369), E356 (= E371)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
38% identity, 95% coverage: 16:381/385 of query aligns to 12:377/381 of 2jifA
- active site: L125 (≠ M131), S126 (= S132), G242 (≠ E246), E363 (≠ A367), K375 (≠ R379)
- binding coenzyme a persulfide: S132 (= S138), S134 (≠ V140), Y178 (≠ S182), Y232 (≠ V236), I236 (≠ M240), L239 (= L243), N240 (≠ D244), R243 (= R247), Y362 (≠ G366), E363 (≠ A367), G364 (= G368), I368 (= I372)
- binding flavin-adenine dinucleotide: F123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), S158 (≠ T164), K201 (= K205), T209 (= T213), R268 (= R272), F271 (= F275), L275 (≠ I279), F278 (= F282), L281 (≠ M285), E336 (≠ Q340), W337 (≠ A341), G340 (= G344), N367 (≠ E371), I368 (= I372)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
38% identity, 95% coverage: 16:381/385 of query aligns to 63:428/432 of P45954
- V137 (≠ L91) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ S92) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 129:138, 70% identical) binding in other chain
- S183 (= S138) binding
- WIS 207:209 (≠ WIT 162:164) binding in other chain
- S210 (≠ N165) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ S182) binding
- L255 (≠ M208) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ V236) binding
- NEGR 291:294 (≠ DYER 244:247) binding
- I316 (≠ L269) to V: in dbSNP:rs1131430
- R319 (= R272) binding
- Q330 (= Q283) binding
- EWMGG 387:391 (≠ QALGG 340:344) binding
- A416 (≠ T369) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TNE 369:371) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
7w0jE Acyl-coa dehydrogenase, tfu_1647
40% identity, 98% coverage: 7:382/385 of query aligns to 1:381/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (= S132), W157 (= W162), R270 (= R272), Q272 (= Q274), F273 (= F275), I277 (= I279), F280 (= F282), I283 (≠ M285), Q339 (= Q340), L340 (≠ A341), G343 (= G344), Y365 (≠ G366), E366 (≠ A367), T368 (= T369), Q370 (≠ E371), I371 (= I372)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
40% identity, 97% coverage: 11:382/385 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S138), T134 (≠ V140), R180 (= R183), R234 (≠ G237), L237 (≠ M240), R238 (≠ S241), L240 (= L243), D241 (= D244), R244 (= R247), E365 (≠ A367), G366 (= G368), R377 (= R379)
- binding flavin-adenine dinucleotide: Y123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (≠ L362), T367 (= T369), Q369 (≠ E371)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
40% identity, 97% coverage: 11:382/385 of query aligns to 7:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (≠ L362), Y364 (≠ G366), T367 (= T369), Q369 (≠ E371)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 98% coverage: 6:383/385 of query aligns to 1:383/389 of C3UVB0
- A80 (≠ S83) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G90) binding
- V88 (≠ L91) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G94) binding
- FGIT 126:129 (≠ LAMS 129:132) binding
- S135 (= S138) binding ; binding
- WIS 159:161 (≠ WIT 162:164) binding
- S181 (= S182) binding
- R271 (= R272) binding
- FQMN 281:284 (≠ FQLM 282:285) binding
- R340 (≠ Q340) binding
- A344 (≠ G344) binding
- V366 (≠ G366) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTNE 367:371) binding
Sites not aligning to the query:
Query Sequence
>Ga0059261_4052 FitnessBrowser__Korea:Ga0059261_4052
MSLPQMDFALSETAEMIRDTTQRFAKERIEPLAAKIDAEDWFPRDELWTAMGELGLHGIT
VDEEFGGLGLGYLEHVIACEEVSRASASIGLSYGAHSNLCVNQISRWASPAQKAKYLPRL
ISGEHVGSLAMSEAGAGSDVVSMKLRAEHKGDRYVLNGTKFWITNAAYADTLVVYAKTGE
GSRGITTFLIEKDMPGFSIGQKIDKMGMRGSPTAELVFDDCEVPEENVMGPLNGGVGVLM
SGLDYERTVLAGIQLGIMQACLDVVLPYLRERKQFGQAIGSFQLMQAKVADMYVALNSAR
AYVYAVAQACDAGKTTRFDAAGAILLASENAFRVAGEAVQALGGAGYTKDWPVERFLRDA
KLLDIGAGTNEIRRMLIGRELIGAA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory